|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
22-174 |
1.42e-48 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 171.24 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFIKTGCSYAVVQVEMKNSGE 101
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTLKNQGL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240258 102 DAfkpeiyggviiierritesatatvlkdylgkkvsnkrdelrelvehfnidveNPCVVMSQDKSREFLHSGN 174
Cdd:cd03276 81 DA----------------------------------------------------NPLCVLSQDMARSFLTSNK 101
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
961-1057 |
2.38e-45 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 162.00 E-value: 2.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 961 DATSNVVRDTKGLSGGERSFSTLCFALALHEMTEAPFRAMDEFDVFMDAVSRKISLDALVDFAIG-EGSQWMFITPHDIS 1039
Cdd:cd03276 98 TSNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKqPGRQFIFITPQDIS 177
|
90
....*....|....*...
gi 15240258 1040 MVKSHERIKKQQMAAPRS 1057
Cdd:cd03276 178 GLASSDDVKVFRMKDPRG 195
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-1010 |
4.51e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.85 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHS-NLQIEFGEWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFIKTG-----CSYAVVQVE 95
Cdd:TIGR02169 2 IERIELENFKSFGkKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGkngqsGNEAYVTVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 96 MKNSGEdAFKPEIyggVIIIERRITESATATVLkdYL-GKKVSnkRDELRELVEHFNIDVENPCVVMSQD---------- 164
Cdd:TIGR02169 82 FKNDDG-KFPDEL---EVVRRLKVTDDGKYSYY--YLnGQRVR--LSEIHDFLAAAGIYPEGYNVVLQGDvtdfismspv 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 165 --------------------KSREFLHSGNDKDKFKFFFKATLLQQVNDL------------------------------ 194
Cdd:TIGR02169 154 errkiideiagvaefdrkkeKALEELEEVEENIERLDLIIDEKRQQLERLrrerekaeryqallkekreyegyellkeke 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 195 ------------LQSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNM---------EQVEEIAQRLQQLKKKLAws 253
Cdd:TIGR02169 234 alerqkeaierqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkEKIGELEAEIASLERSIA-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 254 wvyDVDRQLQEQTEKIVKLKERIPTCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAKTAVREKI 333
Cdd:TIGR02169 312 ---EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 334 ALQEE---FNHKCNYVQ----KIKDRVRRLERQVGDINEQtMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEencf 406
Cdd:TIGR02169 389 DYREKlekLKREINELKreldRLQEELQRLSEELADLNAA-IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD---- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 407 LEKAfegRKKMEHIEDMIKNHQKRQRFITSNINDLKKHQTNKVTAFGGDRVINLLqaiernhrrFRKPPIGPIGSHVTLV 486
Cdd:TIGR02169 464 LSKY---EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV---------LKASIQGVHGTVAQLG 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 487 N-GNKWASSVEQALGTLLNAFIVtdhKDSLTLRGCANEANYRNL---KIIIYDFSRPRLNIPRHMVPQTEHPTIFSVIDS 562
Cdd:TIGR02169 532 SvGERYATAIEVAAGNRLNNVVV---EDDAVAKEAIELLKRRKAgraTFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 563 DN---PTVLNVLVDqsgverQVLAENYEEGKAVAFGKRLSNLK-EVYTLDG------YKMFFRGPVQTTLPPLSRRPSRL 632
Cdd:TIGR02169 609 DPkyePAFKYVFGD------TLVVEDIEAARRLMGKYRMVTLEgELFEKSGamtggsRAPRGGILFSRSEPAELQRLRER 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 633 CASFDDQIKDLEIEASKEQNEINQCMRRKREAEENLEELELKVRQLKKHRSQAEKVLTTKELEMHDLK----------NT 702
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqeienvkselKE 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 703 VAAEIEALpSSSVNELQREI-----MKDLEEIDEKEAFLEKLQN-------CLKEAELKANKLTALFENMRESAKGEIDA 770
Cdd:TIGR02169 763 LEARIEEL-EEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEevsrieaRLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 771 FEEAENELKKIEKDLQSAEAEKIHYENIMKNKVLpDIKNAEANYEELKNKRKESDQKASEICP-----ESEIESLGPWDG 845
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEA-ALRDLESRLGDLKKERDELEAQLRELERkieelEAQIEKKRKRLS 920
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 846 STPEQLSAQITRMNQ--RLHRENQQFSE---SIDDLRMMYESLERKI-----------------AKKRKSYQDHREKLMA 903
Cdd:TIGR02169 921 ELKAKLEALEEELSEieDPKGEDEEIPEeelSLEDVQAELQRVEEEIralepvnmlaiqeyeevLKRLDELKEKRAKLEE 1000
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 904 CKNALDSRWAKFQRnaslLRRQLTWQ-FNAhlgkkgISGHIKVSY---ENKTLSIEVKMPQDATS---NVVRDTKG---- 972
Cdd:TIGR02169 1001 ERKAILERIEEYEK----KKREVFMEaFEA------INENFNEIFaelSGGTGELILENPDDPFAgglELSAKPKGkpvq 1070
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|..
gi 15240258 973 ----LSGGERSFSTLCFALALHEMTEAPFRAMDEFDVFMDAV 1010
Cdd:TIGR02169 1071 rleaMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGV 1112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-927 |
1.29e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.59 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 185 ATLLQQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNMEQ-VEEIAQRLQQLKKKLAwswvyDVDRQLQ 263
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEeIEELQKELYALANEIS-----RLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 264 EQTEKIVKLKERIPTCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAKTAVREKIALQEEfnhkc 343
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 344 nyVQKIKDRVRRLERQVGDINeqtmkntqAEQSEIEEKLKYLEQEVEK----VETLRSRLKEEENCFLEKAFEGRKKMEH 419
Cdd:TIGR02168 381 --LETLRSKVAQLELQIASLN--------NEIERLEARLERLEDRRERlqqeIEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 420 --------IEDMIKNHQKRQRFITSNINDLKKhQTNKVTAfggdrVINLLQAIERNHRRF----------RKPPIGPIGS 481
Cdd:TIGR02168 451 elqeelerLEEALEELREELEEAEQALDAAER-ELAQLQA-----RLDSLERLQENLEGFsegvkallknQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 482 HVTLVN-GNKWASSVEQALGTLLNAFIVTDHKDSLTLRGCANEANYRNLKIIIYDFSRPRLNIPRHMVPQTEHPTIFSV- 559
Cdd:TIGR02168 525 LSELISvDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVa 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 560 -----IDSDNPTVLNVLVDQSgverqVLAENYEEGKAVAfgKRLSNLKEVYTLDGYKMFFRG-----PVQTTLPPLSRRp 629
Cdd:TIGR02168 605 kdlvkFDPKLRKALSYLLGGV-----LVVDDLDNALELA--KKLRPGYRIVTLDGDLVRPGGvitggSAKTNSSILERR- 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 630 srlcasfdDQIKDLE--IEASKEQNEINQcmrrkreaeENLEELELKVRQLKKHRSQAEKVLTTKELEMHDLKNTVA--- 704
Cdd:TIGR02168 677 --------REIEELEekIEELEEKIAELE---------KALAELRKELEELEEELEQLRKELEELSRQISALRKDLArle 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 705 AEIEALpSSSVNELQREIMKDLEEIDEKEAFLEKLQNCLKEAELKANKLTALFENMRESAKGEIDAFEEAENELKKIEKD 784
Cdd:TIGR02168 740 AEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 785 LQSAEAEKIHYENimknkvlpDIKNAEANYEELKNKRKESDQKASEIcpESEIESLgpwdGSTPEQLSAQIT-------R 857
Cdd:TIGR02168 819 AANLRERLESLER--------RIAATERRLEDLEEQIEELSEDIESL--AAEIEEL----EELIEELESELEallneraS 884
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 858 MNQRLHRENQQFSESIDDLRmmyeSLERKIAKKRKSYQDHREKLmackNALDSRWAKFQRNASLLRRQLT 927
Cdd:TIGR02168 885 LEEALALLRSELEELSEELR----ELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQERLS 946
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
20-102 |
9.25e-19 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 86.11 E-value: 9.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 20 GSILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFIKTGCSYAVVQVEMKNS 99
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
...
gi 15240258 100 GED 102
Cdd:cd03277 81 PGN 83
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
973-1051 |
4.25e-14 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 71.57 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 973 LSGGERSFSTLCFALALHEMTEAPFRAMDEFDVFMDAVSRKISLDALVDFAIgEGSQWMFITPHDISMVKSHE--RIKKQ 1050
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAK-HTSQFIVITLKKEMFENADKliGVLFV 173
|
.
gi 15240258 1051 Q 1051
Cdd:cd03239 174 H 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-442 |
1.77e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFIKTGCSYAVVQVEMKNSGE 101
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 102 DafkpeiyggvIIIERRITESaTATVLKDYLGKKVSNKRDELRELVEHF-NIDVENPCVVMSQDKSREFLHSGNDKDKfk 180
Cdd:PRK03918 83 K----------YRIVRSFNRG-ESYLKYLDGSEVLEEGDSSVREWVERLiPYHVFLNAIYIRQGEIDAILESDESREK-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 181 fffkatLLQQVNDL--LQSIYEHLTKataIVDELENTIKPIEKEIS---ELRGKIKNMEQ-VEEIAQRLQQLKKKLawsw 254
Cdd:PRK03918 150 ------VVRQILGLddYENAYKNLGE---VIKEIKRRIERLEKFIKrteNIEELIKEKEKeLEEVLREINEISSEL---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 255 vydvdRQLQEQTEKIVK-------LKERIPTCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMK---REIESFHQS 324
Cdd:PRK03918 217 -----PELREELEKLEKevkeleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKELKELKEK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 325 AKTaVREKIALQEEFNHKCNYVQKIKDRVRR----LERQVGDINEQT--MKNTQAEQSEIEEKLKYLEQEVEKVETLRSR 398
Cdd:PRK03918 292 AEE-YIKLSEFYEEYLDELREIEKRLSRLEEeingIEERIKELEEKEerLEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15240258 399 LKEEENcfLEKAFEGRKKmEHIEDMIKNHQKRQRFITSNINDLK 442
Cdd:PRK03918 371 KEELER--LKKRLTGLTP-EKLEKELEELEKAKEEIEEEISKIT 411
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
940-1048 |
3.47e-12 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 66.85 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 940 SGHIKVSYENKTLSIEVK-----MPQD-----ATSNVV------RDTKGL--------SGGERSFSTLCFALALHEMTEA 995
Cdd:cd03277 70 EGTIEIELYGNPGNIQVDnlcqfLPQDrvgefAKLSPIellvkfREGEQLqeldphhqSGGERSVSTMLYLLSLQELTRC 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15240258 996 PFRAMDEFDVFMDAVSRKISLDALVDFAIGEG-SQWMFITPHDISMVKSHERIK 1048
Cdd:cd03277 150 PFRVVDEINQGMDPTNERKVFDMLVETACKEGtSQYFLITPKLLPGLNYHEKMT 203
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
25-249 |
1.34e-11 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 64.44 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 25 IKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLK------DFIKTGCSYAVVQVEMKN 98
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGfvkgdiRIGLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 99 SGedafkpEIYGGVIIIERRITESATATVLKDYL-GKKVSNKRDELRELVEHFNIDVENpCVVMSQDKSREFLhsgndkd 177
Cdd:pfam13476 81 ND------GRYTYAIERSRELSKKKGKTKKKEILeILEIDELQQFISELLKSDKIILPL-LVFLGQEREEEFE------- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240258 178 kfkfffKATLLQQVNDLLQSIyehltkataivdelentikpieKEISELRGKIKNMEQVEEIAQRLQQLKKK 249
Cdd:pfam13476 147 ------RKEKKERLEELEKAL----------------------EEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
22-99 |
1.49e-11 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 64.25 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQIEFG-EWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKD---FIKTGCSYAVVQVEMK 97
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGsNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLaggGVKAGINSASVEITFD 80
|
..
gi 15240258 98 NS 99
Cdd:cd03239 81 KS 82
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
38-957 |
2.10e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 68.46 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 38 IEFGEWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFI----KTGCSYAVVQVEMKNSGEDAFkpeIYGGVI 113
Cdd:pfam02463 19 LPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsksGAFVNSAEVEITFDNEDHELP---IDKEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 114 IIERRITESATATVLKDylGKKVSNKrdELRELVEHFNIDVENPCVVMSQDKSREFLHSGNDKDKFKFFFKATLLQqvnd 193
Cdd:pfam02463 96 SIRRRVYRGGDSEYYIN--GKNVTKK--EVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRL---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 194 llqsiYEHLTKATAIVDELENTIKPIEKEISELRGKIKNMEQVEEIAQRLQQLKKKLAWSWVYD-VDRQLQEQTEKIVKL 272
Cdd:pfam02463 168 -----KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlYLDYLKLNEERIDLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 273 KERIPTCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAKTAVREKIALQEEFNHKCNYVQKIKDR 352
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 353 VRRLERQvgdINEQTMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEENC-FLEKAFEGRKKMEHIEDMIKNHQKRQ 431
Cdd:pfam02463 323 KKKAEKE---LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEeELLAKKKLESERLSSAAKLKEEELEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 432 RFITSNI---------------NDLKKHQTNKVTAFGGDRVINLLQAIERNHRRFRKPPIGPIGSHVTLVNGNKWASSVE 496
Cdd:pfam02463 400 KSEEEKEaqlllelarqledllKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 497 QALGTLLNAFIVTDHKDSLTLRGCANEANYRNLKIIIYDFSRPRLNIPRHMvpQTEHPTIFSVIDSDNPTVLNVLVDQSG 576
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR--LGDLGVAVENYKVAISTAVIVEVSATA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 577 VERQVLAENYEEGKAVAFGKRLSNLKEVYTLDGYKMFFRGPVQTTLPPLSRRPSRLCASFDDQIKDLEIEASKEQNEINQ 656
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 657 CMRRKREAEENLEELELKVRQLKKHRSQAEKVLTTKELEMHDLKNTVAAEIEALPsssvNELQREIMKDLEEIDEKEAFL 736
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE----EILRRQLEIKKKEQREKEELK 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 737 EKLqncLKEAELKANKLTALFENMRESAKGEIDAFEEAENELKKIEKDLQSAEAEKIHYENIMKNKVLPDIKNAE--ANY 814
Cdd:pfam02463 714 KLK---LEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKlkVEE 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 815 EELKNKRKESDQKASEICPESEIESLGPWDGSTPEQLSAQITRMNQRLHRE----NQQFSESIDDLRMMYESLERKIAKK 890
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALElkeeQKLEKLAEEELERLEEEITKEELLQ 870
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240258 891 RKSYQDHREKLMACKNALDSRWAKFQRNASLLRRQLTWQFNAHLGKKGISGHIKVSYENKTLSIEVK 957
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
22-101 |
7.97e-10 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 59.64 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQ-IEFGEWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAAtlKDFIKTGCSYAVVQVEMKNSG 100
Cdd:COG0419 2 LLRLRLENFRSYRDTEtIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLR--SDLINVGSEEASVELEFEHGG 79
|
.
gi 15240258 101 E 101
Cdd:COG0419 80 K 80
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
971-1035 |
8.22e-10 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 58.53 E-value: 8.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240258 971 KGLSGGERSFSTLCFALALHEMTEAPFRAMDEFDVFMDAVSRKISLDALVDFAIGeGSQWMFITP 1035
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITH 139
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
22-156 |
6.98e-09 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 58.86 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCVAFGcraRGTQRAATLKDFiktgcsyavvqvemkNSGE 101
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLG---PSSSRKFDEEDF---------------YLGD 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 102 DAFKPEIyggVIIIE-----RRITESATATVLKDYLGKKVSNKRDELRELVEHFNIDVEN 156
Cdd:COG3593 65 DPDLPEI---EIELTfgsllSRLLRLLLKEEDKEELEEALEELNEELKEALKALNELLSE 121
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-115 |
7.17e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.85 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMC-HSNLQIEFGEWVNFITGQNGSGKSAILTALCVA-FGCRARGTQRAATLKDFIKTGCSYAVVQVEMKNS 99
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYAlTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENA 80
|
90 100
....*....|....*....|
gi 15240258 100 GEDAFK----PEIYGGVIII 115
Cdd:cd03240 81 NGKKYTitrsLAILENVIFC 100
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
22-174 |
8.20e-09 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 57.98 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCVAFGCRArgtqraatLKDFIKTGCSYAVVQVEMKNSGE 101
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRA--------SADLIRSGAEKAVVEGVFDISDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 102 DAFKP-----EIYGGVIIIERRITESATATVLkdYLGKKVSNK---RDELRELVE----HFNIDvenpcvVMSQDKSREF 169
Cdd:cd03241 73 EEAKAlllelGIEDDDDLIIRREISRKGRSRY--FINGQSVTLkllRELGSLLVDihgqHDHQN------LLNPERQLDL 144
|
....*
gi 15240258 170 LHSGN 174
Cdd:cd03241 145 LDGGL 149
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
22-445 |
1.48e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCVAFgcraRGTQRAATLKDFIKTGCSYAVVQVEMKNSGE 101
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFAL----FTDKRTEKIEDMIKKGKNNLEVELEFRIGGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 102 dafkpeiyggVIIIERRITE-----SATATVLKD--YLGKKVSNKRDELRELVEHFNIDVENPCVVMSQDKSREFLHSGN 174
Cdd:PRK01156 79 ----------VYQIRRSIERrgkgsRREAYIKKDgsIIAEGFDDTTKYIEKNILGISKDVFLNSIFVGQGEMDSLISGDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 175 DKDKFKFFFKATL--LQQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNMEQVEEIAqrlqqLKKKLAW 252
Cdd:PRK01156 149 AQRKKILDEILEInsLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSIT-----LKEIERL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 253 SWVYDVD-----------RQLQEQTEKIVKLKERIPTCQAKIDWELGKVESLRdtltkkkaqvaclmdESTAMKREIESf 321
Cdd:PRK01156 224 SIEYNNAmddynnlksalNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYK---------------ELEERHMKIIN- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 322 hqSAKTAVREKIalqeefNHKCNYVQKIKDRVRRLERQVGDIN--EQTMKNTQAEQSEIEEKLKyLEQEVEKVETLRSRL 399
Cdd:PRK01156 288 --DPVYKNRNYI------NDYFKYKNDIENKKQILSNIDAEINkyHAIIKKLSVLQKDYNDYIK-KKSRYDDLNNQILEL 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15240258 400 KEEENCFLEKAfegrKKMEHIEDMIKNHQKRQRFITSNINDLKKHQ 445
Cdd:PRK01156 359 EGYEMDYNSYL----KSIESLKKKIEEYSKNIERMSAFISEILKIQ 400
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
200-445 |
4.57e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 200 EHLTKATAIVDELENTIKPIEKeiselrgkiknmeQVE------EIAQRLQQLKKKLAWSWVYDVDRQLQEQTEKIVKLK 273
Cdd:COG1196 186 ENLERLEDILGELERQLEPLER-------------QAEkaeryrELKEELKELEAELLLLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 274 ERIPTCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAKTAVREKIALQEEfnhkcnyVQKIKDRV 353
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-------LEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 354 RRLERQVGDINEQtMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEENCFLEKAFEGRKKMEHIEDMIKNHQKRQRF 433
Cdd:COG1196 326 AELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250
....*....|..
gi 15240258 434 ITSNINDLKKHQ 445
Cdd:COG1196 405 LEEAEEALLERL 416
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
21-152 |
5.62e-08 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 55.93 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 21 SILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCV-AFGcraRGTqRAATLKDFIKTGCSYAVVQVEMKNS 99
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLlAPG---RSH-RTARDKELIRFGAEAAVIHGRVEKG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15240258 100 gedafkpeiyGGVIIIERRITESATATVLKDylGKKVSNkrdeLRELVEHFNI 152
Cdd:PRK00064 78 ----------GRELPLGLEIDKKGGRKVRIN--GEPQRK----LAELAGLLNV 114
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-86 |
1.38e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 54.23 E-value: 1.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEW--VNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFIKTG 86
Cdd:COG3950 3 IKSLTIENFRGFEDLEIDFDNPprLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNG 69
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
200-442 |
2.97e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 200 EHLTKATAIVDELENTIKPIEKEISELRGKIKNMEQV----------EEIAQRLQQLKKKLAwswVYDVDrQLQEQTEKI 269
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkeseliklKELAEQLKELEEKLK---KYNLE-ELEKKAEEY 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 270 VKLKERIPTCQAKI---DWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAKTAVREKIALQEEFNHKCNYV 346
Cdd:PRK03918 528 EKLKEKLIKLKGEIkslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLEL 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 347 QKIKDRVRRLERQVGDineqtmkntqaEQSEIEEKLKYLEQEVEKVETLRSRLKEEENCFLEKAFEG--------RKKME 418
Cdd:PRK03918 608 KDAEKELEREEKELKK-----------LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEElreeylelSRELA 676
|
250 260
....*....|....*....|....
gi 15240258 419 HIEDMIKNHQKRQRFITSNINDLK 442
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLK 700
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
24-402 |
3.29e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.25 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 24 RIKVENFMCHSN--LQIEFGEW-VNFITGQNGSGKSAILTALCVA-FGCRARGTQRAATLKDFIKTGCsyaVVQVEMKnS 99
Cdd:PHA02562 6 KIRYKNILSVGNqpIEIQLDKVkKTLITGKNGAGKSTMLEALTFAlFGKPFRDIKKGQLINSINKKDL---LVELWFE-Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 100 GEDAF------KPEIYGgVIIIERRITESATATVLKDYLGK--KVSNKR--------------------DELRELVEhfn 151
Cdd:PHA02562 82 GEKEYyikrgiKPNVFE-IYCNGKLLDESASSKDFQKYFEQmlGMNYKSfkqivvlgtagyvpfmqlsaPARRKLVE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 152 iDVENPCVVMSQDKSREFLHSGNDKDKFKFFFKATLLQQ--------VNDLLQSIYEHLTKATAIVDELENTIKPIEKEI 223
Cdd:PHA02562 158 -DLLDISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQqiktynknIEEQRKKNGENIARKQNKYDELVEEAKTIKAEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 224 SELRGKIKNME-QVEEIAQRLQQLKKKLAwswvyDVDRQLqEQTEKIVKLKER---IPTCQAKIDWELGKVESLRDtltK 299
Cdd:PHA02562 237 EELTDELLNLVmDIEDPSAALNKLNTAAA-----KIKSKI-EQFQKVIKMYEKggvCPTCTQQISEGPDRITKIKD---K 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 300 KKAQVACLMDESTAMKREIESFHQsAKTAVREKIALQEEFNhkcnyvqKIKDRVRRLERQVGDInEQTMKNTQAEQSEIE 379
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDE-FNEQSKKLLELKNKIS-------TNKQSLITLVDKAKKV-KAAIEELQAEFVDNA 378
|
410 420
....*....|....*....|...
gi 15240258 380 EKLKYLEQEVEKVETLRSRLKEE 402
Cdd:PHA02562 379 EELAKLQDELDKIVKTKSELVKE 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
188-443 |
3.38e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 188 LQQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNM-EQVEEIAQRLQQLKKKLAWS--WVYDVDRQLQE 264
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLnEEAANLRERLESLERRIAATerRLEDLEEQIEE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 265 QTEKIVKLKERIPTCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAKTAVREKIALQEEFNHKCN 344
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 345 YVQKIKDRVRRLERQVGDINEQTMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLkeeencflekafeGRKKMEHIEDmI 424
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL-------------GPVNLAAIEE-Y 995
|
250
....*....|....*....
gi 15240258 425 KNHQKRQRFITSNINDLKK 443
Cdd:TIGR02168 996 EELKERYDFLTAQKEDLTE 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-413 |
1.53e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 24 RIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCVA-FGCRARGTqraaTLKDFIKTGCSYAVVQVEMKNSGED 102
Cdd:PRK02224 5 RVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEACFFAlYGSKALDD----TLDDVITIGAEEAEIELWFEHAGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 103 afkpeiyggvIIIERRI---TESATAT--VLKDYLGkKVSNKRDELRELVEHFNIDVE-----------------NPCVV 160
Cdd:PRK02224 81 ----------YHIERRVrlsGDRATTAkcVLETPEG-TIDGARDVREEVTELLRMDAEafvncayvrqgevnkliNATPS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 161 MSQDKSREFLHSGNDKDKFKFFFKATLlqQVNDLLQSIYEHLTKATAIVDELENT-----IKPIEKEISELRGKIKNME- 234
Cdd:PRK02224 150 DRQDMIDDLLQLGKLEEYRERASDARL--GVERVLSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEe 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 235 QVEEIAQRLQQLKKKLAwswvydvdrQLQEQTEKIVKLKERIPTCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAM 314
Cdd:PRK02224 228 QREQARETRDEADEVLE---------EHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 315 --KREIESFHQSAKTAVREKIALQEEfnhkcnyvqKIKDRVRRLERQVGDINEQTMKNTQA------EQSEIEEKLKYLE 386
Cdd:PRK02224 299 laEAGLDDADAEAVEARREELEDRDE---------ELRDRLEECRVAAQAHNEEAESLREDaddleeRAEELREEAAELE 369
|
410 420 430
....*....|....*....|....*....|...
gi 15240258 387 QEVEK----VETLRSRLKE--EENCFLEKAFEG 413
Cdd:PRK02224 370 SELEEareaVEDRREEIEEleEEIEELRERFGD 402
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
45-165 |
1.54e-06 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 50.76 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 45 NFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFI----KTGCSYAVVQVEMKNS--GEDAFKPEIYgGVIIIERR 118
Cdd:cd03273 28 NAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIykrgQAGITKASVTIVFDNSdkSQSPIGFENY-PEITVTRQ 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15240258 119 ITESATatvlKDYL--GKKVSNKRdeLRELVEHFNIDVENPCVVMSQDK 165
Cdd:cd03273 107 IVLGGT----NKYLinGHRAQQQR--VQDLFQSVQLNVNNPHFLIMQGR 149
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-95 |
4.23e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 4.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240258 24 RIKVENFMCH-SNLQIEFGE-WVNFITGQNGSGKSAILTALCVAFGcrarGTQRAATLKDFIKTGCSYAVVQVE 95
Cdd:cd03227 1 KIVLGRFPSYfVPNDVTFGEgSLTIITGPNGSGKSTILDAIGLALG----GAQSATRRRSGVKAGCIVAAVSAE 70
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
22-152 |
4.93e-06 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 49.22 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTAlcVAFGCRARGtQRAATLKDFIKTGCSYAVVQVEMKNSge 101
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEA--ISLLATGKS-HRTSRDKELIRWGAEEAKISAVLERQ-- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15240258 102 dafkpeiyGGVIIIERRITESAtatvlkdylGKKVSNKRDELR---ELVEHFNI 152
Cdd:cd03242 76 --------GGELALELTIRSGG---------GRKARLNGIKVRrlsDLLGVLNA 112
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
167-430 |
1.01e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 167 REFLHSGNDKDKFKFFFKATLLQQVNDLLQSIYEhLTKATAIVDELENTIKPIEKEISELRGKIKNMEQVEEIAQRLQQL 246
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 247 KKKLAWSWVYDVDRQLQEQTEKIVKLKERIPTCQAKIDWELGKVESLRDTLTK-KKAQVAC------LMDESTamKREIE 319
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElKKAKGKCpvcgreLTEEHR--KELLE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 320 SFHQSAKTAVREKIALQEEfnhkcnyVQKIKDRVRRLERQVGDINEQTMKNTQAEQ-SEIEEKLKY-----LEQEVEKVE 393
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEK-------ERKLRKELRELEKVLKKESELIKLKELAEQlKELEEKLKKynleeLEKKAEEYE 528
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15240258 394 TLRSRLKEEE------NCFLEKAFEGRKKMEHIEDMIKNHQKR 430
Cdd:PRK03918 529 KLKEKLIKLKgeikslKKELEKLEELKKKLAELEKKLDELEEE 571
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
205-443 |
1.04e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 205 ATAIVDELENTIKPIEKEISELRGKIKNME-QVEEIAQRLQQLKKKLAwswvyDVDRQLQEQTEKIVKLKERIPTCQAKI 283
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKkEEKALLKQLAALERRIA-----ALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 284 dwelgkvESLRDTLTKKKAQVACLMDESTAMKReiesfhqsaktavREKIAL---QEEFNhkcnyvqkikDRVRRLE--R 358
Cdd:COG4942 93 -------AELRAELEAQKEELAELLRALYRLGR-------------QPPLALllsPEDFL----------DAVRRLQylK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 359 QVGDINEQTMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEENcFLEKAFEGRKK-MEHIEDMIKNHQKRQRFITSN 437
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-ALEALKAERQKlLARLEKELAELAAELAELQQE 221
|
....*.
gi 15240258 438 INDLKK 443
Cdd:COG4942 222 AEELEA 227
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
188-448 |
1.05e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 188 LQQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEIS-----------ELRGKIKNMEQVEEIAQRLQQLKKKLAwSWVY 256
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensekqrELEEKQNEIEKLKKENQSYKQEIKNLE-SQIN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 257 DVDRQLQEQTEKIVKLKERIPTCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESfHQSAKTAVREKIalq 336
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN-LDNTRESLETQL--- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 337 EEFNHKCNYV-QKIKDRVRRLERQVGDINEQTMKNTQAEQ--SEIEEKLKYLEQEVEKVETLRSR----LKEEENCFLEK 409
Cdd:TIGR04523 471 KVLSRSINKIkQNLEQKQKELKSKEKELKKLNEEKKELEEkvKDLTKKISSLKEKIEKLESEKKEkeskISDLEDELNKD 550
|
250 260 270
....*....|....*....|....*....|....*....
gi 15240258 410 AFEgrKKMEHIEDMIKNHQKRQRFITSNINDLKKHQTNK 448
Cdd:TIGR04523 551 DFE--LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-403 |
1.11e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 188 LQQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNME-QVEEIAQRLQQLKKKLAwswvyDVDRQLQEQT 266
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEqELAALEAELAELEKEIA-----ELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 267 EkivKLKERIPTCQAkidweLGKVESLRDTLTKKKAQVACLMDE-----STAMKREIESFHQSAKTAVREKIALQEEFNH 341
Cdd:COG4942 104 E---ELAELLRALYR-----LGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240258 342 KCNYVQKIKDRVRRLERQVGDiNEQTMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEE 403
Cdd:COG4942 176 LEALLAELEEERAALEALKAE-RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
22-101 |
1.17e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 47.65 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQ-IEF----GEWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFIKTGCSYAVVQVEM 96
Cdd:cd03279 3 PLKLELKNFGPFREEQvIDFtgldNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFTF 82
|
....*
gi 15240258 97 KNSGE 101
Cdd:cd03279 83 QLGGK 87
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
189-450 |
1.48e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 189 QQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEISEL---RGKIKNME-QVEEIAQRLQQLKKKLAWSWVYDVDRQLQE 264
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnNKKIKELEkQLNQLKSEISDLNNQKEQDWNKELKSELKN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 265 QTEKIVKLKERIPTCQAKIDwelgkveSLRDTLTKKKAQVACLMDESTAMKREIESFHQSAKTAVREKIALQEEfnhkcn 344
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIIS-------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE------ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 345 yVQKIKDRVRRLERQVGDINEQT------MKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEENCFLEKAFEGRKKME 418
Cdd:TIGR04523 386 -IKNLESQINDLESKIQNQEKLNqqkdeqIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
250 260 270
....*....|....*....|....*....|..
gi 15240258 419 HIEDMIKNHQKRQRFITSNINDLKKHQTNKVT 450
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
22-245 |
1.53e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 48.92 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTALCVAFGCRARgtqraatlKDFIKTGCSYAVVQVEMKNSGE 101
Cdd:COG0497 2 LTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRAD--------ASLVRHGADKAEVEAVFDLSDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 102 DAFKP-------EIYGGVIIIERRITES-----------ATATVLKDyLGkkvsnkrdelRELV------EHFNIdvenp 157
Cdd:COG0497 74 PPLAAwleenglDLDDGELILRREISADgrsrafingrpVTLSQLRE-LG----------ELLVdihgqhEHQSL----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 158 cvvMSQDKSREFL--HSGNdkdkfkfffkATLLQQVNDL------LQSIYEHLTKATA-----------IVDELENtIKP 218
Cdd:COG0497 138 ---LDPDAQRELLdaFAGL----------EELLEEYREAyrawraLKKELEELRADEAerareldllrfQLEELEA-AAL 203
|
250 260
....*....|....*....|....*..
gi 15240258 219 IEKEISELRGKIKNMEQVEEIAQRLQQ 245
Cdd:COG0497 204 QPGEEEELEEERRRLSNAEKLREALQE 230
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
164-375 |
2.31e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 164 DKSREFLHSGNDKDKFKFFFKATLLQQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNMEQVEEIAQRL 243
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 244 QQLKKklawswvydVDRQLQEQTEKIVKLKERIPTCQAKIDwelgKVESLRDTLTKKKAQVACLMDESTAMKReiesfhQ 323
Cdd:COG4717 132 QELEA---------LEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATE------E 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15240258 324 SAKTAVREKIALQEEFNHKCNYVQKIKDRVRRLERQVGDINEQTMKNTQAEQ 375
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
637-892 |
2.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 637 DDQIKDLEIEASKEQNEINQCMRRKREAEENLEELELKVRQLKKHRSQaekvLTTKELEMHDLKNTVAAEIEALPS--SS 714
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE----IEELEKELESLEGSKRKLEEKIREleER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 715 VNELQREI------MKDLEEIDEKEAFLEKLQNCLKEAELKANKLTALFENMRESAKG---EIDAFEEAENELKKIEKDL 785
Cdd:PRK03918 268 IEELKKEIeeleekVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieeRIKELEEKEERLEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 786 QSAEAEKIHYENimKNKVLPDIKNAEANYEELKNKRKesdqkaseicpeseieslgpwdGSTPEQLSAQItrmnQRLHRE 865
Cdd:PRK03918 348 KELEKRLEELEE--RHELYEEAKAKKEELERLKKRLT----------------------GLTPEKLEKEL----EELEKA 399
|
250 260
....*....|....*....|....*..
gi 15240258 866 NQQFSESIDDLRMMYESLERKIAKKRK 892
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKK 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
188-505 |
3.52e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 188 LQQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNME-QVEEIAQRLQQLKKKLAwswvyDVDRQLQEQT 266
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELElELEEAQAEEYELLAELA-----RLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 267 EKIVKLKERIptcqAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIE-SFHQSAKTAVREKIALQEEFNHKCNY 345
Cdd:COG1196 309 ERRRELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEaELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 346 VQKIKDRVRRLERQVGDIN--EQTMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEENCFLEKAFEGRKKMEHIEDM 423
Cdd:COG1196 385 AEELLEALRAAAELAAQLEelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 424 IKNHQKRQRFITSNINDLKKHQTNKVtafggdRVINLLQAIERNHR------RFRKPPIGPIGSHVTLVNGNKWASSVEQ 497
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAA------ARLLLLLEAEADYEgflegvKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
....*...
gi 15240258 498 ALGTLLNA 505
Cdd:COG1196 539 ALEAALAA 546
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
22-62 |
4.02e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 47.23 E-value: 4.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEwVNFITGQNGSGKSAILTAL 62
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDAL 41
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
209-412 |
4.95e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 209 VDELENTIKPIEKEISELRGKIKNMEQVE----EIAQRLQQLKKKL---AWSWVYDVDRQLQEqTEKIVKLKERIPTCQA 281
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKLAELEkkldELEEELAELLKELeelGFESVEELEERLKE-LEPFYNEYLELKDAEK 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 282 KIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQsaKTAVREKIALQEEFNHKCNYVQKIKDRVRRLERQVG 361
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15240258 362 DInEQTMKNTQAEQSEIEEK---LKYLEQEVEKVETLRSRLKEEENCFLEKAFE 412
Cdd:PRK03918 691 EI-KKTLEKLKEELEEREKAkkeLEKLEKALERVEELREKVKKYKALLKERALS 743
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
219-432 |
1.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 219 IEKEISEL-----RGKIKNMEQVEEIAQRLQQLKKKLawswvydvdRQLQEQTEKIVKLKERIPTCQAKIDwelgKVESL 293
Cdd:COG4717 51 LEKEADELfkpqgRKPELNLKELKELEEELKEAEEKE---------EEYAELQEELEELEEELEELEAELE----ELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 294 RDTLTKKKaQVACLMDESTAMKREIESFHQSAKTAVREkialQEEFNHKCNYVQKIKDRVRRLERQVGDINEQTMKNTQA 373
Cdd:COG4717 118 LEKLEKLL-QLLPLYQELEALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15240258 374 EQSEIEEKLKYLEQEVEKVETLRSRLKEEENcflekafEGRKKMEHIEDMIKNHQKRQR 432
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELE-------ELEEELEQLENELEAAALEER 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-431 |
1.18e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 234 EQVEEIAQRLQQLKKKLAwswvyDVDRQLQEQTEKIVKLKERIPTCQAKIDwelgkveSLRDTLTKKKAQVACLMDEsta 313
Cdd:COG3883 23 KELSELQAELEAAQAELD-----ALQAELEELNEEYNELQAELEALQAEID-------KLQAEIAEAEAEIEERREE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 314 MKREIESFHQSAKTAVREKIALQ----EEFNHKCNYVQKIKDRVRRLerqvgdineqtMKNTQAEQSEIEEKLKYLEQEV 389
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADL-----------LEELKADKAELEAKKAELEAKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15240258 390 EKVETLRSRLKEEENCFLEKAFEGRKKMEHIEDMIKNHQKRQ 431
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
210-402 |
2.04e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 210 DELENTIKPIEKEISELRGKIKNME-QVEEIAQRLQQLKKKLAwswvyDVDRQLQEQTEKIVKLKERiptcqakidweLG 288
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEaRLEAAKTELEDLEKEIK-----RLELEIEEVEARIKKYEEQ-----------LG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 289 KVESLRdtltkkkaqvaclmdESTAMKREIESFHQSAKTAVREKIALQEEFNHKCNYVQKIKDRVRRLERQVgdineqtm 368
Cdd:COG1579 84 NVRNNK---------------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL-------- 140
|
170 180 190
....*....|....*....|....*....|....
gi 15240258 369 kntQAEQSEIEEKLKYLEQEVEKVETLRSRLKEE 402
Cdd:COG1579 141 ---EEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
22-1036 |
3.01e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQ-IEFGEWVNF--ITGQNGSGKSAILTALCVAF--GCRARGtQRAATLKDFIKTGCSYAVVQVEM 96
Cdd:TIGR00618 3 PLRLTLKNFGSYKGTHtIDFTALGPIflICGKTGAGKTTLLDAITYALygKLPRRS-EVIRSLNSLYAAPSEAAFAELEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 97 knsgedAFKPEIYGGVIIIERRITESATATVLKDYLGKK-------VSNKRDELRELVEHFNIDVEN--PCVVMSQDKSR 167
Cdd:TIGR00618 82 ------SLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKkgrgrilAAKKSETEEVIHDLLKLDYKTftRVVLLPQGEFA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 168 EFLHSgNDKDKFKFFFKATLLQQVNDLLQSIYEHL----TKATAIVDELENTIKPIEKEISELRGKIKNME-QVEEIAQR 242
Cdd:TIGR00618 156 QFLKA-KSKEKKELLMNLFPLDQYTQLALMEFAKKkslhGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEkELKHLREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 243 LQQLKKKLAWswvYDVDRQLQEQTEKIVKLKERIPTCQAKIDWELGKVESLRDTLTKKKaQVACLMDESTAMKrEIESFH 322
Cdd:TIGR00618 235 LQQTQQSHAY---LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRAR-KAAPLAAHIKAVT-QIEQQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 323 QSAKTAVREKIALQEEFNHKCNYVQKikdrvRRLERQVGDINEQTMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEE 402
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVK-----QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 403 ENcFLEKAFEGRKKMEHIEDMIKNHQKRQRFITSNINDLKKHqtnKVTAFGGDRVINLLQAIERNHrrFRKPPIGPIGSH 482
Cdd:TIGR00618 385 QQ-QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQ---LAHAKKQQELQQRYAELCAAA--ITCTAQCEKLEK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 483 VTLVNGNKWASSVEQALGTllnafivtdhKDSLTLRgcaneanYRNLKIIIYDFSRPRLNIPRHMVPQTEHPTIfSVIDS 562
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQT----------KEQIHLQ-------ETRKKAVVLARLLELQEEPCPLCGSCIHPNP-ARQDI 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 563 DNPTVLNVLVDQSGVERQVLAENYE--EGKAVAFGKRLSNLKEVYTLdgykmffrgpVQTTLPPLSRRPSRLCASFDDQI 640
Cdd:TIGR00618 521 DNPGPLTRRMQRGEQTYAQLETSEEdvYHQLTSERKQRASLKEQMQE----------IQQSFSILTQCDNRSKEDIPNLQ 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 641 K---------DLEIEASKEQNEINQCMRRKREAEENLEELELKVRQLKKHRSQAEKVLTTKELEMHDLKNTVAA-EIEAL 710
Cdd:TIGR00618 591 NitvrlqdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAlSIRVL 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 711 PSSSVNELQREIMKDLEEIDEKEAFLEKLQNC---LKEAELKANKLTALFE---NMRESAKGEIDAFEEAENELKKIEKD 784
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKEQLTYWKEMLAQCqtlLRELETHIEEYDREFNeieNASSSLGSDLAAREDALNQSLKELMH 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 785 LQSAEAEKIHYENIMKNKVLPDIKNAEANYEELK----NKRKESDQKASEICP-ESEIESLGPWDGSTPEQLSAQITRMN 859
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAaeiqFFNRLREEDTHLLKTlEAEIGQEIPSDEDILNLQCETLVQEE 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 860 QRLHRENQQFSESIDDLRMMYESLERKIAKKRKSYQDHREKLMACKNALDSRWAKFQRNASLLRR---QLTWQFNAHLGK 936
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKflhEITLYANVRLAN 910
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 937 KG-ISGHIKVSYENKTLS---IEVKMPQDATSNVVRDTKGLSGGERSFSTLCFALALHEMTEAPFRA------MDEFDVF 1006
Cdd:TIGR00618 911 QSeGRFHGRYADSHVNARkyqGLALLVADAYTGSVRPSATLSGGETFLASLSLALALADLLSTSGGTvldslfIDEGFGS 990
|
1050 1060 1070
....*....|....*....|....*....|
gi 15240258 1007 MDAVSRKISLDALVdfAIGEGSQWMFITPH 1036
Cdd:TIGR00618 991 LDEDSLDRAIGILD--AIREGSKMIGIISH 1018
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-403 |
3.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 33 HSNLQIEFGEWVNFITGQNGSGKS----AILTALC----VAF-------------------GCRARGTQRAATLKDFIKT 85
Cdd:COG4913 15 DGVHTIDFDGRGTLLTGDNGSGKStlldAIQTLLVpakrPRFnkaandagksdrtllsyvrGKYGSERDEAGTRPVYLRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 86 GCSYAVVQVEMKNSGED-------AFkpEIYGGV----------IIIERRITESA--------TATVLKDYLGKKV---- 136
Cdd:COG4913 95 GDTWSAIAATFANDGSGqtvtlaqVF--WLKGDAsslgdvkrffVIADGPLDLEDfeefahgfDIRALKARLKKQGveff 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 137 SNKRDELRELVEHFNIDVENPCVVMSQDKSreflhsgndkdkfkfffkatlLQQVNDLLQSIYEH-------LTKATAIV 209
Cdd:COG4913 173 DSFSAYLARLRRRLGIGSEKALRLLHKTQS---------------------FKPIGDLDDFVREYmleepdtFEAADALV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 210 DELEnTIKPIEKEISELRGKIKNMEQVEEIAQRLQQLKKKLAwSWVYDVDR-QLQEQTEKIVKLKERIPTCQAKIDWELG 288
Cdd:COG4913 232 EHFD-DLERAHEALEDAREQIELLEPIRELAERYAAARERLA-ELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 289 KVESLRDTLTKKKAQVaclmdesTAMKREIESFHQSAKTAVREKIA-LQEEfnhkcnyVQKIKDRVRRLERQVGDI---- 363
Cdd:COG4913 310 ELERLEARLDALREEL-------DELEAQIRGNGGDRLEQLEREIErLERE-------LEERERRRARLEALLAALglpl 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15240258 364 --NEQTMKNTQAE----QSEIEEKLKYLEQEVEKVETLRSRLKEEE 403
Cdd:COG4913 376 paSAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRREL 421
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
713-926 |
3.36e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 713 SSVNELQREIMKDLEEIDEKEAFLEKLQNCLKEAELkaNKLTAlFENMRESAKGEIDAFEEAENELKKIEK--------- 783
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEI--NKSIN-EYNKIESARADLEDIKIKINELKDKHDkyeeiknry 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 784 ---DLQSAEAEKIHYENIMKNKVLPDIKNAEANYEELKNKRKESDQKASEIcpESEIESLGPWDGSTpeqlsaqITRMNQ 860
Cdd:PRK01156 556 kslKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEI--EIGFPDDKSYIDKS-------IREIEN 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240258 861 RLHRENQQFSEsIDDLRMMYESLERKIA--KKRKSYQDHREKlmaCKNALDSRWAKFQRNASLLRRQL 926
Cdd:PRK01156 627 EANNLNNKYNE-IQENKILIEKLRGKIDnyKKQIAEIDSIIP---DLKEITSRINDIEDNLKKSRKAL 690
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
22-62 |
4.14e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 44.13 E-value: 4.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSAILTAL 62
Cdd:pfam13175 3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEAL 43
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
38-138 |
4.25e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.45 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 38 IEFGEWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFI------KTGCSYAVVQVEMKNSGedafkpEIYGg 111
Cdd:cd03278 18 IPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIfagsetRKPANFAEVTLTFDNSD------GRYS- 90
|
90 100
....*....|....*....|....*..
gi 15240258 112 vIIIERRITESATATvlkdylGKKVSN 138
Cdd:cd03278 91 -IISQGDVSEIIEAP------GKKVQR 110
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
22-170 |
4.50e-04 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 42.94 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQ-IEFGEWVNFITGQNGSGKSAILTALCVAFGCRARgTQRAATLKDFIKTGC-------SYAVVQ 93
Cdd:cd03275 1 LKRLELENFKSYKGRHvIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSS-HLRSKNLKDLIYRARvgkpdsnSAYVTA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240258 94 VEMKNSGEDAFkpeiyggviiIERRITESATatvlkDYL--GKKVSnkRDELRELVEHFNIDVenpcvvmsqdKSREFL 170
Cdd:cd03275 80 VYEDDDGEEKT----------FRRIITGGSS-----SYRinGKVVS--LKEYNEELEKINILV----------KARNFL 131
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
219-431 |
5.02e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 219 IEKEISELRGKIKNMEQVEEIAQRLQQLKKKL----------------AWSWVYDVDRQLQEQTEKIVKLKERIPTCQAK 282
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLrkvveeltakkmtlesSERTVSDLTASLQEKERAIEATNAEITKLRSR 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 283 IDWELGKVESLR---DTLTKKKAQVACLMDESTA-------MKREIESFHQ-------SAKTAVREKIALQEEFNHKCNY 345
Cdd:pfam15921 526 VDLKLQELQHLKnegDHLRNVQTECEALKLQMAEkdkvieiLRQQIENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 346 VQKIK-------DRVRRLERQVGDINEQTMKNTQAeQSEIEEKLKYLEQE----VEKVETLRSRLKE--EENCFLEKAFe 412
Cdd:pfam15921 606 LQEFKilkdkkdAKIRELEARVSDLELEKVKLVNA-GSERLRAVKDIKQErdqlLNEVKTSRNELNSlsEDYEVLKRNF- 683
|
250
....*....|....*....
gi 15240258 413 gRKKMEHIEdMIKNHQKRQ 431
Cdd:pfam15921 684 -RNKSEEME-TTTNKLKMQ 700
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-441 |
5.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 185 ATLLQQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNM-EQVEEIAQRLQQLKKKLAwswvyDVDRQLQ 263
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkEELKALREALDELRAELT-----LLNEEAA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 264 EQTEKIVKLKERIPTCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAKTAVREKIALQEEFNHKC 343
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 344 NYVQKIKDRVRRLERQvgdineqtMKNTQAEQSEIEEKLKYLEQEvekVETLRSRLKEEENCFLEKAFEgrkKMEHIEDM 423
Cdd:TIGR02168 901 EELRELESKRSELRRE--------LEELREKLAQLELRLEGLEVR---IDNLQERLSEEYSLTLEEAEA---LENKIEDD 966
|
250
....*....|....*...
gi 15240258 424 IKNHQKRQRFITSNINDL 441
Cdd:TIGR02168 967 EEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
639-926 |
5.88e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 639 QIKDLEIEASKEQNEINQCMRRKREAEEnleelelKVRQLKKHRSQAEKVLTTKELEMHDLKNTVAAEIealpsSSVNEL 718
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELEELELELEEAQAEEYELL-----AELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 719 QREIMKDLEEIDEKEAFLEKLQNCLKEAELKANKLTALFENMRESAKGEIDAFEEAENELKKIEKDLQSAEAEKIHYENi 798
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 799 mknkvlpdiKNAEANYEELKNKRKESDQKASEICPESEIESLgpwdgstpEQLSAQITRMNQRLHRENQQFSESIDDLRM 878
Cdd:COG1196 380 ---------ELEELAEELLEALRAAAELAAQLEELEEAEEAL--------LERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15240258 879 -------MYESLERKIAKKRKSYQDHREKLMACKNALDSRWAKFQRNASLLRRQL 926
Cdd:COG1196 443 aleeaaeEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
187-421 |
5.95e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 187 LLQQVNDLLQSIYEHLTKATAIVDE---LENTIKPIEKEISELRG-KIKNMEQVEEIAQRLQQL---KKKL--AWSWVYD 257
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEkaqLEKEINDRRLELQEFKIlKDKKDAKIRELEARVSDLeleKVKLvnAGSERLR 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 258 VDRQLQEQTEKIVKlkeRIPTCQAKI-----DWEL------GKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAK 326
Cdd:pfam15921 647 AVKDIKQERDQLLN---EVKTSRNELnslseDYEVlkrnfrNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDG 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 327 TAVREKIALQEEFNHKCNYVQKIKDRVRRLErqvgdineQTMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEENCF 406
Cdd:pfam15921 724 HAMKVAMGMQKQITAKRGQIDALQSKIQFLE--------EAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL 795
|
250
....*....|....*
gi 15240258 407 LEKAFEGRKKMEHIE 421
Cdd:pfam15921 796 RSQERRLKEKVANME 810
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
200-404 |
6.77e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 200 EHLTKATAIVDELENTIKPIEKEISELRgkiknmEQVEEIAQRLQQLKKKLAwswvyDVDRQLQEQTEKIVKLKERIPTC 279
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIAERR------ETIEEKRERAEELRERAA-----ELEAEAEEKREAAAEAEEEAEEA 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 280 Q---AKIDWELGKVESLRDTLTKkkaqVACLMDESTAMKREIESfhqsaktaVREKI-ALQEEFNHKCNYVQKIKDRVRR 355
Cdd:PRK02224 571 ReevAELNSKLAELKERIESLER----IRTLLAAIADAEDEIER--------LREKReALAELNDERRERLAEKRERKRE 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240258 356 LERQVGD--INEQTMKNTQAE--QSEIEEKLKYL--------------EQEVEKVETLRSRLKEEEN 404
Cdd:PRK02224 639 LEAEFDEarIEEAREDKERAEeyLEQVEEKLDELreerddlqaeigavENELEELEELRERREALEN 705
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
951-1021 |
8.01e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.53 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 951 TLSIEVKMPQDATSNVVRDTKGLSGGERSFST-LCFALAL------HEMTEAPFR--AMDEfdVF--MDAVSRKISLDAL 1019
Cdd:pfam13558 11 SFEVEVRDEDGSEVETYRRSGGLSGGEKQLLAyLPLAAALaaqygsAEGRPPAPRlvFLDE--AFakLDEENIRTALELL 88
|
..
gi 15240258 1020 VD 1021
Cdd:pfam13558 89 RA 90
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
668-927 |
8.05e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 668 LEELELKV----RQLKKHRSQAEKvlTTKELEMHDLKNTVAAEIEALpssSVNELQREIMKDLEEIDEKEAFLEKLQNCL 743
Cdd:TIGR02168 188 LDRLEDILneleRQLKSLERQAEK--AERYKELKAELRELELALLVL---RLEELREELEELQEELKEAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 744 KEAELKANKLTALFENMRESAKGEIDAFEEAENELKKIEKDLQSAEAEKIHYENimknkvlpDIKNAEANYEELKNKRKE 823
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER--------QLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 824 SDQKASEIcpESEIESLgpwdgstpEQLSAQITRMNQRLHRENQQFSESIDDLRMMYESLERKIAKKRKSYQDHREKLM- 902
Cdd:TIGR02168 335 LAEELAEL--EEKLEEL--------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIEr 404
|
250 260
....*....|....*....|....*..
gi 15240258 903 --ACKNALDSRWAKFQRNASLLRRQLT 927
Cdd:TIGR02168 405 leARLERLEDRRERLQQEIEELLKKLE 431
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
678-901 |
8.28e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 678 LKKHRSQAEKVLTTKELEMHDLK---NTVAAEIEALP-SSSVNELQREIMKDLEEIDEKEAFLEKLQnclKEAELKANKL 753
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRqknGLVDLSEEAKLlLQQLSELESQLAEARAELAEAEARLAALR---AQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 754 TALFENmresakgeiDAFEEAENELKKIEKDLqsAEAEKIHYENimknkvLPDIKNAEANYEELKNK-RKESDQKASEIc 832
Cdd:COG3206 257 PELLQS---------PVIQQLRAQLAELEAEL--AELSARYTPN------HPDVIALRAQIAALRAQlQQEAQRILASL- 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240258 833 pESEIESLGpwdgSTPEQLSAQITRMNQRLHRENQQFSEsiddlrmmYESLERKIAKKRKSYQDHREKL 901
Cdd:COG3206 319 -EAELEALQ----AREASLQAQLAQLEARLAELPELEAE--------LRRLEREVEVARELYESLLQRL 374
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
677-831 |
8.87e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 677 QLKKHRSQAEKVLTTKELEMHDLKNTVAAEIEALpSSSVNELQREIMKDLEEIDEKEAFLEKLQNCLKEAELKANKLtal 756
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETEEELQQQREEELEEL-QEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEEL--- 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240258 757 fENMRESAKGEIDAFEEAENELKKIEKDLQSAEAEKIHYENIMKNKVLPDIKNAEANYEELKNKRKESDQKASEI 831
Cdd:pfam05667 383 -EKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEI 456
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
196-426 |
1.06e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 196 QSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNMEQVEEIAQRLQQLkkklawswvyDVDRQLQEQTEKIVKLKER 275
Cdd:PRK05771 82 KSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNF----------DLDLSLLLGFKYVSVFVGT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 276 IP---TCQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIEsFHQSAKTAVREKIALQEEfnhkcnyVQKIKDR 352
Cdd:PRK05771 152 VPedkLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELK-KLGFERLELEEEGTPSEL-------IREIKEE 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240258 353 VRRLERQVGDINEQTMKNTQAEQSEIEEKLKYLEQEVEKVETLrSRLKEEENCFlekAFEG---RKKMEHIEDMIKN 426
Cdd:PRK05771 224 LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEAL-SKFLKTDKTF---AIEGwvpEDRVKKLKELIDK 296
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
674-1043 |
1.14e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 674 KVRQLKKHRSQAEKVLTTKELEMHDLKNTVAAEIEAlpsssvnELQREIMKDLEE-IDEKEAFLEKLQNCLKEAELKANK 752
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRI-------ERLEERREDLEElIAERRETIEEKRERAEELRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 753 LTALFENMRESAKGEIDAFEEAENELKKIEKDLQSAEAEKIHYENImkNKVLPDIKNAEANYEELKNKRKE----SDQKA 828
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERI--RTLLAAIADAEDEIERLREKREAlaelNDERR 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 829 SEICPESE-IESL-GPWDGSTPEQLSAQITRMNQRLhrenQQFSESIDDLRMMYESLERKIA------KKRKSYQDHREK 900
Cdd:PRK02224 627 ERLAEKRErKRELeAEFDEARIEEAREDKERAEEYL----EQVEEKLDELREERDDLQAEIGavenelEELEELRERREA 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 901 LMACKNALDS---------------RWAKFQRNASLLRRQLTWQFNAHLGKKGISgHIKVSYENKtLSIEVKmpqDATSn 965
Cdd:PRK02224 703 LENRVEALEAlydeaeelesmygdlRAELRQRNVETLERMLNETFDLVYQNDAYS-HIELDGEYE-LTVYQK---DGEP- 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 966 vvRDTKGLSGGERSFSTLCFALALHEMT------EAPFRAM--DEFDVFMDA--VSRkisLDALVDFAIGEGSQWMFITP 1035
Cdd:PRK02224 777 --LEPEQLSGGERALFNLSLRCAIYRLLaegiegDAPLPPLilDEPTVFLDSghVSQ---LVDLVESMRRLGVEQIVVVS 851
|
....*...
gi 15240258 1036 HDISMVKS 1043
Cdd:PRK02224 852 HDDELVGA 859
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
209-391 |
1.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 209 VDELENTIKPIEKEISELRGKIKNMEQVEEIAQRLQQlkkkLAWSwvyDVDrqLQEQTEKIVKLKERIptcqAKIDWELG 288
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAE----YSWD---EID--VASAEREIAELEAEL----ERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 289 KVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAKTAVREKIALQEEFNhkcNYVQKIKDRVR-----RLERQVGDI 363
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRalleeRFAAALGDA 762
|
170 180
....*....|....*....|....*....
gi 15240258 364 NEQTM-KNTQAEQSEIEEKLKYLEQEVEK 391
Cdd:COG4913 763 VERELrENLEERIDALRARLNRAEEELER 791
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
219-447 |
1.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 219 IEKEISELRGKIKNMEQVEEIAQRLQQLKKKlawswvyDVDRQLQEQTEKIVKLKERIPTCQAKIDWELGKVESLRDTLT 298
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-------EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 299 KKKAQVACLMDESTAMKREIESFHQSA--KTAVREKIALQEEFNHKCNYVQKIK-DRVRRLERQVGDINEQTMKNTQAEQ 375
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEedEKKAAEALKKEAEEAKKAEELKKKEaEEKKKAEELKKAEEENKIKAEEAKK 1737
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240258 376 SEIEEKLKYLEQEVEKVEtlRSRLKEEENCFLEKAFEGRKKMEHI--EDMIKNHQKRQRFITSNINDLKKHQTN 447
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEE--KKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
973-1044 |
1.43e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.91 E-value: 1.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240258 973 LSGGERSFSTLCFALALHEMTEAPFRAMDEFDVFMDA--VSRKISLdaLVDFAigEGSQWMFITPHDISMVKSH 1044
Cdd:cd03278 114 LSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDanVERFARL--LKEFS--KETQFIVITHRKGTMEAAD 183
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
200-404 |
1.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 200 EHLTKATAIVDELENTIKPIEKEISELRGKIKNM-EQVEEIAQRLQQLKKKLAWSWVYD--VDRQLQEQTEKIVKLKERI 276
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLrERLEELEEERDDLLAEAGLDDADAeaVEARREELEDRDEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 277 PTCQAKIDWELGKVESLRDTLTKKKAQVACLMDEStamkREIESFHQSAKTAVREKIALQEEfnhkcnyvqkIKDRVRRL 356
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEA----AELESELEEAREAVEDRREEIEE----------LEEEIEEL 396
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15240258 357 ERQVGDINEQtmknTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEEN 404
Cdd:PRK02224 397 RERFGDAPVD----LGNAEDFLEELREERDELREREAELEATLRTARE 440
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
38-72 |
1.85e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 41.29 E-value: 1.85e-03
10 20 30
....*....|....*....|....*....|....*
gi 15240258 38 IEFGEWVNFITGQNGSGKSAILTALCVAFGCRARG 72
Cdd:COG3910 33 LEFHPPVTFFVGENGSGKSTLLEAIAVAAGFNPEG 67
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
22-62 |
1.88e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 41.49 E-value: 1.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEwVNFITGQNGSGKSAILTAL 62
Cdd:COG4938 1 IKSISIKNFGPFKEAELELKP-LTLLIGPNGSGKSTLIQAL 40
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
204-403 |
1.91e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 204 KATAIVDEL-----ENTIKPIEKEISELRGKIKnmEQVEEIAQRLQQLKKKLAW----SWVYDVDRQLQEQTEKIVKLKE 274
Cdd:COG3206 149 LAAAVANALaeaylEQNLELRREEARKALEFLE--EQLPELRKELEEAEAALEEfrqkNGLVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 275 RIptcqAKIDWELGKVESLRDTLTKKKAQVACLMDESTAmKREIESFHQSAKTAVREKIALQEEFNHKCNYVQKIKDRVR 354
Cdd:COG3206 227 QL----AEARAELAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15240258 355 RLERQVGDINEQTMKNTQAEQSEIEEKLKYLEQEVEKVETLRSRLKEEE 403
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
636-829 |
2.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 636 FDDQIKDLEIEASKEQNEINQCMRRKREAE--ENLEELELKVRQLKKHRSQAEKVLTTKELEMHDLKNTVAAEIEALPSS 713
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 714 SVNELQREIMKDLEEIDEKEAFL---------------EKLQNCLKEAELKANKLTALFENMRESAKGEIDAFEEAENEL 778
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELsarytpnhpdvialrAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15240258 779 KKIEKDLQSAEAEkihYENIMKnkvlpDIKNAEANYEELKNKRKESDQKAS 829
Cdd:COG3206 340 EARLAELPELEAE---LRRLER-----EVEVARELYESLLQRLEEARLAEA 382
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
22-217 |
2.73e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 41.18 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMC-HSNLQIEFGEW------VNFITGQNGSGKSAILTALcvafgcrargtqraATLKDFIKTGCSYAVVQV 94
Cdd:COG1106 2 LISFSIENFRSfKDELTLSMVASglrllrVNLIYGANASGKSNLLEAL--------------YFLRNLVLNSSQPGDKLV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 95 E-MKNSGEDAFKPEIYGGVIIIERRITE---SATATVLKD----YLGKKVSNKRDELRELVEHFNIDVEnpcvvmsqdks 166
Cdd:COG1106 68 EpFLLDSESKNEPSEFEILFLLDGVRYEygfELDKERIISewlyFLSTAAQLNVPLLSPLYDWFDNNIS----------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15240258 167 refLHSGNDKDKFKFFFKATLLQQVNDLLQSIYEHLTKATAIVDELENTIK 217
Cdd:COG1106 137 ---LDTSSDGLTLLLKEDESLKEELLELLKIADPGIEDIEVEEEEIEDLVE 184
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
22-303 |
3.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 22 ILRIKVENFMCHSNLQIEFGEWVNFITGQNGSGKSailtalcvafgcrargtqraaTLKDFIKtgcsyAVVQVEMKNSGE 101
Cdd:COG4717 3 IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKS---------------------TLLAFIR-----AMLLERLEKEAD 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 102 DAFKPEIYGGVIIIERRitesatatvlkdylgKKVSNKRDELRELVEHFNIDVEnpcvvmSQDKSREFLHSGNDKDKFKF 181
Cdd:COG4717 57 ELFKPQGRKPELNLKEL---------------KELEEELKEAEEKEEEYAELQE------ELEELEEELEELEAELEELR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 182 FFKATLLQQVNDL-----LQSIYEHLTKATAIVDELENTIKPIEKEISELRGKIKNMEQVEEIAQRLQQLKKKLAWSWVY 256
Cdd:COG4717 116 EELEKLEKLLQLLplyqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15240258 257 DVDRQLQEQTEKIVKLKERIPTCQAKIDWELGKVESLRDTLTKKKAQ 303
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
697-926 |
3.53e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 697 HDLKNTVAAEIEALpSSSVNELQRE--------IMKDLEEIDEK-EAFLEKLQNC-LKEAELKANKLTALFENMRESAKG 766
Cdd:pfam06160 203 EELKTELPDQLEEL-KEGYREMEEEgyalehlnVDKEIQQLEEQlEENLALLENLeLDEAEEALEEIEERIDQLYDLLEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 767 EIDAFEEAENELKKIEKDLQSAEAE----KIHYENIMKNKVLPDikNAEANYEELknkrkesdqkaseicpESEIeslgp 842
Cdd:pfam06160 282 EVDAKKYVEKNLPEIEDYLEHAEEQnkelKEELERVQQSYTLNE--NELERVRGL----------------EKQL----- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 843 wdgstpEQLSAQITRMNQRLHRENQQFSESIDDLRMMYESLErKIAKKRKSYQDH----REKLMACKNALDsrwaKFQRN 918
Cdd:pfam06160 339 ------EELEKRYDEIVERLEEKEVAYSELQEELEEILEQLE-EIEEEQEEFKESlqslRKDELEAREKLD----EFKLE 407
|
....*...
gi 15240258 919 ASLLRRQL 926
Cdd:pfam06160 408 LREIKRLV 415
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
973-1042 |
4.27e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.15 E-value: 4.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 973 LSGGERSFSTLCFALALhemtEAPFRAMDEFDVFMDAVSRKISLDALVDFAiGEGSQWMFITpHDISMVK 1042
Cdd:cd00267 81 LSGGQRQRVALARALLL----NPDLLLLDEPTSGLDPASRERLLELLRELA-EEGRTVIIVT-HDPELAE 144
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
674-786 |
4.70e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 674 KVRQLKKHRSQAEKVLTtkelemHDLKNTVAAEIealPSSSVNELQREIMKDLEEIDEK-EAFLEKLQNcLKEAELKANK 752
Cdd:PRK04778 349 SVRQLEKQLESLEKQYD------EITERIAEQEI---AYSELQEELEEILKQLEEIEKEqEKLSEMLQG-LRKDELEARE 418
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15240258 753 LTALFENMRESAKGE-------------IDAFEEAENELKKIEKDLQ 786
Cdd:PRK04778 419 KLERYRNKLHEIKRYleksnlpglpedyLEMFFEVSDEIEALAEELE 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
637-927 |
5.70e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 637 DDQIKDLEIEASKEQ--NEINQCMRRKREaeenleelelKVRQLKKHRSQAEKVLTTKELEmhDLKNTVAAEIEALpsss 714
Cdd:COG1196 199 ERQLEPLERQAEKAEryRELKEELKELEA----------ELLLLKLRELEAELEELEAELE--ELEAELEELEAEL---- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 715 vNELQREIMKDLEEIDEKEAFLEKLQNCLKEAELKANKLTALFENMRESAKGEIDAFEEAENELKKIEKDLQSAEAEKIH 794
Cdd:COG1196 263 -AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 795 YENimknkvlpDIKNAEANYEELKNKRKESDQKASEIcpESEIESLgpwdgstpEQLSAQITRMNQRLHRENQQFSESID 874
Cdd:COG1196 342 LEE--------ELEEAEEELEEAEAELAEAEEALLEA--EAELAEA--------EEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15240258 875 DLRMMYESLERKIAKKRKSYQDHREKLMACKNALDSRWAKFQRNASLLRRQLT 927
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
188-338 |
7.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 188 LQQVNDLLQSIYEHLTKATAIVDELENTIKPIEKEISELRgkiknmEQVEEIAQRLQQ--------------------LK 247
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR------EELGERARALYRsggsvsyldvllgsesfsdfLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 248 KKLAWSWVYDVDRQ-LQEQTEKIVKLKERiptcQAKIDWELGKVESLRDTLTKKKAQVACLMDESTAMKREIESFHQSAK 326
Cdd:COG3883 120 RLSALSKIADADADlLEELKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
|
170
....*....|..
gi 15240258 327 TAVREKIALQEE 338
Cdd:COG3883 196 AQLAELEAELAA 207
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-384 |
7.98e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 186 TLLQQVNDLLQSiyehLTKATAIVDELENTIKPIEKEISELRGKIKNMEQ---VEEIAQRLQQLKKKLAwswvyDVDRQL 262
Cdd:COG3206 216 LLLQQLSELESQ----LAEARAELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELA-----ELSARY 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240258 263 QEQTEKIVKLKERIPTCQAKIDWELGKVeslrdtLTKKKAQVACLMDESTAMKREIESFHQSAKTavrekialqeefnhk 342
Cdd:COG3206 287 TPNHPDVIALRAQIAALRAQLQQEAQRI------LASLEAELEALQAREASLQAQLAQLEARLAE--------------- 345
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15240258 343 cnyVQKIKDRVRRLERQVgDINEQTMKN--TQAEQSEIEEKLKY 384
Cdd:COG3206 346 ---LPELEAELRRLEREV-EVARELYESllQRLEEARLAEALTV 385
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
958-1008 |
9.39e-03 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 38.82 E-value: 9.39e-03
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....*....|....*....|....*....|....*....|....*....|.
gi 15240258 958 MPQDATSNVvrdtKGLSGGERSFSTLCFALALHEMTEAPFRAMDEFDVFMD 1008
Cdd:cd03274 117 MPKKSWKNI----SNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALD 163
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